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10.1126/science.aav4809 http://scihub22266oqcxt.onion/10.1126/science.aav4809 30467180!6459600!30467180     free     free     free       Science 2018 ; 362 (6421): ? Nephropedia Template TP {{tp|p=30467180|t=2018. Structures and gating mechanism of human TRPM2 |pdf=|usr=}}{{30467180}} gab.com Text Structures and gating mechanism of human TRPM2 JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=30467180 #FOAvip Transient receptor potential (TRP) melastatin 2 (TRPM2) is a cation channel associated with numerous diseases. It has a C-terminal NUDT9 homology (NUDT9H) domain responsible for binding adenosine diphosphate (ADP)-ribose (ADPR), and both ADPR and calcium (Ca(2+)) are required for TRPM2 activation. Here we report cryo-electron microscopy structures of human TRPM2 alone, with ADPR, and with ADPR and Ca(2+) NUDT9H forms both intra- and intersubunit interactions with the N-terminal TRPM homology region (MHR1/2/3) in the apo state but undergoes conformational changes upon ADPR binding, resulting in rotation of MHR1/2 and disruption of the intersubunit interaction. The binding of Ca(2+) further engages transmembrane helices and the conserved TRP helix to cause conformational changes at the MHR arm and the lower gating pore to potentiate channel opening. These findings explain the molecular mechanism of concerted TRPM2 gating by ADPR and Ca(2+) and provide insights into the gating mechanism of other TRP channels. Twit Text FOAVip Structures and gating mechanism of human TRPM2 ????Science http://www.kidney.de/pget.php?&tw=1&pmid=30467180 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30467180 #FOAvip English Wikipedia <ref>{{Cite pmid|30467180}}</ref> Structures and gating mechanism of human TRPM2 #MMPMID30467180 Wang L; Fu TM; Zhou Y; Xia S; Greka A; Wu H Science 2018[Dec]; 362 (6421): ? PMID30467180show ga Transient receptor potential (TRP) melastatin 2 (TRPM2) is a cation channel associated with numerous diseases. It has a C-terminal NUDT9 homology (NUDT9H) domain responsible for binding adenosine diphosphate (ADP)-ribose (ADPR), and both ADPR and calcium (Ca(2+)) are required for TRPM2 activation. Here we report cryo-electron microscopy structures of human TRPM2 alone, with ADPR, and with ADPR and Ca(2+) NUDT9H forms both intra- and intersubunit interactions with the N-terminal TRPM homology region (MHR1/2/3) in the apo state but undergoes conformational changes upon ADPR binding, resulting in rotation of MHR1/2 and disruption of the intersubunit interaction. The binding of Ca(2+) further engages transmembrane helices and the conserved TRP helix to cause conformational changes at the MHR arm and the lower gating pore to potentiate channel opening. These findings explain the molecular mechanism of concerted TRPM2 gating by ADPR and Ca(2+) and provide insights into the gating mechanism of other TRP channels. |*Ion Channel Gating[MESH] |Adenosine Diphosphate Ribose/metabolism[MESH] |Calcium/metabolism[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |Pyrophosphatases/chemistry[MESH]Structures and gating mechanism of human TRPM2 (epmc).pdf DeepDyve Pubget Overpricing